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文献和实验Characterization of Calcium Channel Binding
Figure 1.25.1 (A ) Saturation binding of [3 H]PN200‐100 to L‐type calcium channels in mouse heart membrane preparation ( n = 2). (B ) Scatchard analysis of the specific binding data: K d = 54.9 pM and B max = 116.4 fmol/mg protein
Purification and Structure of L-Type Calcium Channels
Calcium channels are an essential part of the cellular signal trans duction system, since they produce changes in cytosolic calcium. Three types of voltage-dependent calcium channels (T, L, and N channels) have been identified
Expression of Extracellular N-Terminal Domain of NMDA Receptor in Mammalian Cells
, exhibit many of the key properties found in native channels including the direct permeability of calcium, voltage-dependent Mg2+ blockade of the ion channel, and binding sites for modulators, such as Zn2+ , glycine, and polyamines (2 ). The NR1 subunit
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